PURIFICATION AND IMMOBILIZATION OF L-ASPARAGINASE ENZYME FROM THE THERMOPHILIC BACTERIA Bacillus licheniformis STRAIN HSA3-1a

L-Asparaginase gives a great benefit in the cancer treatment, especially in acute\ud lymphoblastic leukemia. L-Asparaginase is also proven to reduce the acrylamide\ud content in the foods. The objective of this study was to perform immobilization and\ud characterization L-Asparaginase produced from Bacillus licheniformis Strain HSA3-\ud 1a. The results showed that the free form L-Asparaginase from B.\ud licheniformis HSA3-1a has optimum activity at pH 8 and 50oC, with a specific activity\ud of 616.26 IU/mg protein and stabilized at the optimum pH and temperature for 60\ud minutes. The immobilized L-Asparaginase with activated glutaraldehyde-carbon\ud carrier has optimum activity at pH 7 and 60??C with a specific activity of 499.27 IU/mg\ud protein and stabilized at the optimum pH and temperature for 60 minutes. The\ud immobilized L-Asparaginase can retain its activity by 84.79% after 2 times repeated\ud use

PRODUCTION AND CHARACTERIZATION OF CHITINASE ENZYMES FROM SULILI HOT SPRING IN SOUTH SULAWESI, Bacillus sp. HSA,3-1a

Chitinase is an extracellular enzyme which is capable in hydrolyzing insoluble chitin to its oligomeric and monomeric components. The enzyme produced by thermophilic bacteria was screened and isolated from Sulili hot spring in Pinrang, South Sulawesi, Indonesia. The gram positive spore forming rod shape bacteria was identified as\ud Bacillus sp. HSA,3-1a through morphological and physiological analysis. The production of chitinase enzyme was conducted at various concentration of colloidal chitin at a pH of 7.0 and a temperature of 55 ??C. The bacteria optimally was produced the enzyme at a colloidal chitin concentration of 0.5% after 72 h of incubation. The optimum temperature, pH and substrate concentration of chitinase were 60 ??C, 7.0 and 0.3%, respectively. The enzyme was stable at a pH of 7.0 and a temperature of 60 ??C after 2 h of incubation. The chitinase activities was increased by addition of 1 mM Mg2+, Ca2+ and Mn2+ ions, whereas the activities were decreased by 1 mM Co2+, Fe2+ and Zn2 ions.The molecular weight of the crude enzyme was determined using SDS-PAGE analysis. Five protein fractions were obtained from SDS-PAGE, with MWs of 79, 71, 48, 43 and 22 kDa

Optimasi Produksi dan Karakterisasi Sifat Biokimiawi Enzim Glukanase dari B. licheniformis HSA3-1a Asal Sumber Air Panas, Sulawesi Selatan

Enzim glukanase merupakan enzim ekstraseluler yang dapat menghidrolisis karbahidrat golongan glukan. Glukan merupakan struktur penting penyusun dinding sel jamur, khususnya jamur patogen tanaman. Penelitian ini bertujuan mengisolasi dan mencari kondisi optimum produksi glukanase dari bakteri termofil Bacillus licheniformis HSA3-1a yang diisolasi dari salah satu sumber air panas di Sulawesi Selatan, selanjutnya mengarakterisasi sifat bikimiawi glukanase tersebut. Isolasi enzim glukanase dari isolat B. licheniformis HSA3-1a dimulai dengan penyiapan inokulum, kemudian melakukan optimasi produksi glukanase. Selanjutnya dilakukan uji karakteristik sifat biokimia glukanase menggunakan substrat laminarin 1% pada berbagai variasi suhu, pH dan melakukan penentuan senyawa kofaktor yang dapat bersifat sebagai aktivator atau inhibitor terhadap aktivitas glukanase. Hasil penelitian menunjukkan bahwa enzim glukanase dari B. licheniformis HSA3-1a dapat diproduksi maksimum pada jam ke-96 waktu fermentasi dengan kondisi: konsentrasi substrat (laminarin) 1%, suhu 500C, pH medium 7,0. Karakteristik sifat glukanase adalah enzim ini bekerja optimum pada suhu 50oC dengan pH 8,0, yang diaktifkan oleh ion logam Cu2+, Ni2+ dan Co2+ 5 mM serta dihambat oleh ion Zn2+ 5 mM

THE EFFECT OF Fe2+ DAN Mn2+ IONS TOWARD -CAROTENE PRODUCTIVITY BY PHYTOPLANKTON Isochrysis aff galbana (T-iso)

The research aimed to find out the effect of Fe2+ and Mn2+ towards -carotene productivity as result of oxidative stress from photosystem (PS II). The phytoplanton Isocrysis aff galbana (T-iso) were the microalgae species which had the high lipid content primarily and had potentiality to produce -carotene as the -carotene\ud supplement. Analysis method was carried out by the sonication extraction for short and cheap in the lysis cell of phytoplankton biomassa, infra red (IR) to find out the interaction metal ion and UV/VIS spectrophotometer to determine -carotene concentration. The research result indicateds that Fe2+ has higher impact than Mn2+ on the -carotene productivity. The interaction of ions metal indicates as M-N, -O-M and M OH-C complex in the phytoplankton amino acid. The -carotene concentration is 4,97 ??g/g DW in addition Fe2+ 0,30 ppm and 1,95 ??g/g DW in Mn2+ 0,20 ppm. The dry weight concentrations of -carotene indicates that I. aff galbana with Fe2+ addition has potential as -carotene supplement

Isolasi Kitin dari Limbah Udang Putih (Penaeus merguiensis) Secara Enzimatis

Udang merupakan biota laut yang memiliki nilai ekonomi yang tinggi sehingga banyak dibudidayakan di Indonesia. Salah satu jenis udang yang banyak dibudidayakan adalah jenis udang putih (Penaeus merguiensis). Keberadaan udang putih sebagai salah satu komoditas ekspor unggulan menjadikan permintaan udang keluar negeri cukup tinggi. Proses ekspor udang dilakukan dalam keadaan beku (tanpa kulit dan kepala). Dari hasil pembekuan 40-50% dari bobot udang menghasilkan limbah berupa kulit dan kepala yang tidak dapat dimanfaatkan seluruhnya sehingga dapat mengganggu lingkungan. Penelitian ini tentang isolasi kitin dari limbah kulit udang putih melalui tahap demineralisasi, dekolorisasi dan deproteinasi. Proses demineralisasi dilakukan dengan menggunakan HCl 1,0 M, lalu dilanjutkan dengan proses dekolorisasi dengan menggunakan NaOCl 0,5%. Untuk tahap akhir isolasi kitin dilakukan tahap deproteinasi dengan enzim protease yang diekskresikan oleh Bakteri Bacillus licheniformis HSA3-1a. Dari proses tersebut, diperoleh senyawa kitin dengan kadar air 2,95%, kadar abu 0,55%, kadar N-total 7,45% dan N-Deasetilasi 57,25%

EKSPLORASI DAN KARAKTERISASI BAKTERI TERMOFIL PENGHASIL ENZIM AMILASE DARI SUMBER AIR PANAS PANGGO, SULAWESI SELATAN

Bakteri termofil yang banyak ditemukan pada sumber air panas berpotensi menghasilkan enzim hidrolitik. Salah satu enzim golongan hidrolitik adalah amilase, enzim ini yang dapat menghidrolisis pati menjadi oligomer dan dimernya. Penelitian ini bertujuan untuk eksplorasi dan identifikasi bakteri penghasilkan enzim amilase dari sumber air panas Panggo, kemudian memproduksi dan mengarakterisasi amilase tersebut. Tahapan yang dilakukan dalam penelitian ini meliputi isolasi dan identifikasi bakteri dari sumber air panas Panggo, optimasi produksi dan karakterisasi sifat biokimiawi enzim amilase. Hasil penelitian menunjukkan bahwa eksplorasi bakteri dari sumber air panas Panggo diperoleh 6 (enam) isolat bakteri yang memiliki aktivitas amilase: 3 (tiga) isolat diantaranya yang menunjukkan ciri Bacillus sp (isolat A1, A2 dan B1) yang tumbuh dengan baik pada suhu 50oC, dan 3 (tiga) isolat lainnya yang menunjukkan ciri Enterobacter aglomerans (isolat B2, C1, dan C2) yang hanya tumbuh pada suhu 37oC. Isolat A2 yang teridentifikasi sebagai Bacillus sp merupakan isolat pilihan yang memproduksi amilase maksimum pada waktu fermentasi 48 jam dengan konsentrasi substrat (pati) 1%, pH medium 7,0 dan suhu inkubasi 50oC dengan aktivitas amilase 0,012803 U/mL. Dan pada kondisi yang sama isolat A1 dapat memproduksi amilase maksimum pada waktu fermentasi yang berbeda yaitu 56 jam dengan aktivitas enzim amilase 0,00276 U/mL

Enzymatic Production of Chitosan from theWhite ShrimpWaste (Penaeus merguiensis) and Its Applicationas Preservatives in Fishery Products

Production of chitosan from white shrimp waste (Penaeus merguiensis) enzymatically with protease and chitin deacetylase. These both enzymes are a group of hydrolytic enzymes that could potentially be used in the processing of fish waste that contains protein and chitin. This study aims to produce chitosan enzymatic and applied as a natural preservative in fishery products especially fresh mackerel. The results showed that the enzyme protease and chitin deacetylase from bacteria B. licheniformis HSA3- 1a can be used in producing enzymatic chitosan. The value of the enzymatic characteristics of chitin-total N content = 7.56%, water = 2.85%, ash content = 0.94% and the texture / color in the form of white powder and the value of the degree of chitin deacetylase (DD%) is 42.4 1%.Medium value of the characteristics of chitosan-total N content = 7.34%, water content = 2.11%, ash content = 0.2 1% and the texture / color in the form of white powder and the value of the degree of chitin deacetylase (DD%) was 74, 94% (included in the standard chitosan). The results of the application of chitosan as a\ud preservative in fresh mackerel at various concentrations, suggests that chitosan can be used as a preservative enzymatically at a concentration of 2.5% during the next 24 hours with TPC value = 6.8 x 103 CFU; TVB value = 10 045 mg/100 grams of material, and the results of organoleptic test showed that fish consumption is still in decent condition

PENGARUH SENYAWA KOFAKTOR DAN STABILITAS TERHADAP AKTIVITAS ENZIM ??-1,3- GLUKANASE DARI ISOLAT BAKTERI TERMOFIL Bacillus licheniformis HSA3-1a

Study on the effect of compound cofactor and stability to enzyme activity of ??-1, 3-glucanase has been done. This study used bacterial isolates B. licheniformis HSA3-1a isolated from a hot spring Sulili Pinrang as a source of the enzyme ??-1 ,3-glucanase. Isolation of enzyme made after bacterial are activated and cultured in fermentation medium, pH 7,0 and temperature of 50 0C for 4 days. The resulting enzyme performed activity assay. Activity of enzyme assays performed by adding the compound cofactor MgCl2, CaCl2, CuCl2, CoCl2, and ZnCl2 at different concentrations (0.25, 0.5, and 1.0) mM. To determine the stability of the enzyme made by varying the incubation time (0, 30, 60, 90, 120 and 180) minutes. The result showed that the cofactors of compounds that can serve as an activator for the enzyme ??-1 ,3-glucanase from B. licheniformis HSA3-1a is MgCl2 and CaCl2 at a concentration of 0:25 mM, 0.5 mM and 1.0 mM. Compound cofactor of CaCl2 1 mM is stabilizier of enzyme ??-1,3-glukanase because therelative activity of the enzyme remaining 86% of the treatment time for 180 minutes prainkubasi

PRODUCTION OF PROTEASE ENZYME FROM BACTERIA IN HOT SPRING OF SOUTH SULAWESI, Bacillus licheniformis HSA3-1a

Bacillus licheniformis HSA3-1a is able to produce extracellular protease. The aim of this research was to find out its production optimum time, consentration of MnCl2, temperature and optimum pH, also the cofactor influence on activity protease from B. licheniformis HSA3-1a. The protease activity was tested with a modified method of Walter. Protease production time was optimum for 36 hours with an activity value of 0,394 U/mL, protein content was 132,35 mg/mL. The Optimum condition of protease enzyme were pH 7,0 and temperature 45 ⁰C with an activity value of 0,0463 U/mL. Protease activity could be inhibited by MnCl2 concentration of 0,01 - 0,03 M

PRODUKSI DAN APLIKASI KITINASE DARI B. licheniformis HSA3-1a DALAM MENGHIDROLISIS KITIN DARI LIMBAH UDANG DAN DINDING SEL JAMUR Ganoderma sp.

Kitinase merupakan enzim golongan hidrolitik yang dapat menghidrolisis kitin dari berbagai\ud sumber. Kitinase ini mempunyai aplikasi komersial dalam bidang pertanian dan kesehatan.\ud Produksi kitinase dari B. licheniformis HSA3-1a dilakukan secara ekstraseluler pada kondisi\ud optimum, kemudian kitinase tersebut diaplikasikan dalam menghidrolisis kitin dari limbah\ud udang dan kitin pada jamur Ganoderma sp. penyebab penyakit busuk batang pada kelapa\ud sawit. Hasil penelitian menunjukkan bahwa bakteri B. licheniformis HSA3-1a potensial\ud menghasilkan kitinase yang diproduksi maksimum pada kondisi waktu fermentasi 72 jam,\ud konsentrasi koloidal kitin 0,5%, suhu 55oC dengan nilai aktivitas 0,225 U/mL. Kemampuan\ud kitinase dalam menghidrolisis kitin dari limbah udang ditunjukkan dengan hasil pengujian\ud aktivitas enzim yang menggunakan substrat kitin dari limbah udang dengan aktivitas 0,48\ud Unit/mL dan pola tekstur kitin sebelum dan sesudah hidrolisis terlihat berbeda yang dianalisis\ud dengan menggunakan SEM (Scanning Electron Microscope). Kitinase juga dapat\ud menghidrolisis kitin pada dinding sel jamur Ganoderma sp., hal ini ditunjukkan dengan\ud adanya zona inhibisi disekitar koloni setelah diinkubasi 48 jam sebesar 19,5 mm